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Evolutionary genomics of Colias Phosphoglucose Isomerase (PGI) introns.

Journal of molecular evolution (2012-03-06)
Baiqing Wang, J Mason Depasse, Ward B Watt
ABSTRACT

Little is known of intron sequences' variation in cases where eukaryotic gene coding regions undergo strong balancing selection. Phosphoglucose isomerase, PGI, of Colias butterflies offers such a case. Its 11 introns include many point mutations, insertions, and deletions. This variation changes with intron position and length, and may leave little evidence of homology within introns except for their first and last few basepairs. Intron position is conserved between PGIs of Colias and the silkmoth, but no intron sequence homology remains. % GC content and length are functional properties of introns which can affect whole-gene transcription; we find a relationship between these properties which may indicate selection on transcription speed. Intragenic recombination is active in these introns, as in coding sequences. The small extent of linkage disequilibrium (LD) in the introns decays over a few hundred basepairs. Subsequences of Colias introns match subsequences of other introns, untranslated regions of cDNAs, and insect-related transposons and pathogens, showing that a diverse pool of sequence fragments is the source of intron contents via turnover due to deletion, recombination, and transposition. Like Colias PGI's coding sequences, the introns evolve reticulately with little phylogenetic signal. Exceptions are coding-region allele clades defined by multiple amino acid variants in strong LD, whose introns are closely related but less so than their exons. Similarity of GC content between introns and flanking exons, lack of small introns despite mutational bias toward deletion, and findings already mentioned suggest constraining selection on introns, possibly balancing transcription performance against advantages of higher recombination rate conferred by intron length.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Phosphoglucose Isomerase from rabbit muscle, Type XI, lyophilized powder, ≥200 units/mg protein
Sigma-Aldrich
Phosphoglucose Isomerase from baker′s yeast (S. cerevisiae), Type III, ammonium sulfate suspension, ≥400 units/mg protein (biuret)
Sigma-Aldrich
Phosphoglucose Isomerase from Bacillus stearothermophilus, lyophilized powder, 300-1,000 units/mg protein
Supelco
Phosphoglucose Isomerase from baker′s yeast (S. cerevisiae), for use with Fructose Assay Kit FA-20